High impact information on pkc-2

• DKF-1 phosphorylation and activation are unaffected when PKC activity is eliminated by inhibitors [1].
• Four conserved proteins, including a disabled protein (DAB-1), a vav family GEF (VAV-1), a protein kinase C (PKC-1), and a STAM homolog (PQN-19), function with the VAB-1 Eph/MSP receptor in oocytes [2].
• Highly-selective expression of certain PKC2 isoforms was observed in distinct subsets of neurons, intestinal and muscle cells [3].
• PKC2 mRNAs also incorporate one of two 3'-terminal exons via alternative splicing [3].
• However, the modes of action of Munc-18 and PKC in vesicle transport have not been clarified [4].

Biological context of pkc-2

• Disruption of the PKC2 protein-coding region, deleting the entire catalytic domain of the encoded enzyme, is not lethal to yeast growing on rich media [5].
• On the other hand, protein kinase C (PKC) stimulates Ca2+-dependent exocytosis in various types of secretory cells [4].
• During a large-scale screen of a human fetal brain cDNA library, a novel human gene GNB2L1 encoding a novel RACK (receptor of activated protein kinase C) protein was isolated and sequenced [6].
• We begin with a brief background on the historical use of phorbol esters as tools to decipher the role of the enzyme protein kinase C in signal transduction cascades [7].

Anatomical context of pkc-2

• The expression of pkc-1 seems to be specific to neurons, while that of pkc-2 is detected in several types of cells including neurons and muscle cells [8].
• Here, we show that recombinant Munc-18 is phosphorylated by conventional PKC in a Ca2+- and phospholipid-dependent manner in a cell-free system [4].
• A pathway regulated by protein kinase C (PKC1) also responds to changes in osmolarity and cell wall integrity [9].

Associations of pkc-2 with chemical compounds

• It thus appears that Ca(2+) and PKC are critically involved in GAR-3b-mediated cAMP formation [10].
• Inhibition of protein kinase C (PKC) by chronic treatment with phorbol 12-myristate 13-acetate (PMA) or by GF109203X decreased carbachol-stimulated cAMP production by as much as 68% [10].

Analytical, diagnostic and therapeutic context of pkc-2

• Cells that are capable of receiving and propagating signals carried by Ca2+/diacylglycerol were identified by assessing activities of pkc-2 gene promoters in transgenic C. elegans and visualizing the distribution of PKC2 polypeptides via immunofluorescence [3].
• The gene was deduced to code for a protein kinase C (PKC) homologue by molecular cloning [11].
• Animal models in the study of protein kinase C isozymes [12].

References